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Literature summary for 2.3.1.85 extracted from

  • Wong, H.; Mattick, J.S.; Wakil, S.J.
    The architecture of the animal fatty acid synthetase. III. Isolation and characterization of beta-ketoacyl reductase (1983), J. Biol. Chem., 258, 15305-15311.
    View publication on PubMed
Search for more literature for 2.3.1.85

Inhibitors

Inhibitors Comment Organism Structure
aryl-acyl-beta-alanyl NADP+ inhibits beta-ketoacyl-reductase Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0041
-
 NADPH
-
 Gallus gallus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 molecular weight of fragments after proteolytic cleavage Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2 beta-ketoacyl reductase containing fragments after sequential proteolysis Gallus gallus

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoate + 8 CoA + 7 CO2 + 14 NADP+ + 6 H2O structure and regulation Gallus gallus
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2
-
 NADPH Gallus gallus
2.6
-
 NADPH Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+
-
 Gallus gallus palmitate + 8 CoA + 7 CO2 + 14 NADP+ + 6 H2O
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Gallus gallus

Cofactor

Cofactor Comment Organism Structure
NADPH requirement, high specificity Gallus gallus